ID A0A1R1D405_9BACL Unreviewed; 263 AA.
AC A0A1R1D405;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN ORFNames=BK133_15680 {ECO:0000313|EMBL:OMF31670.1};
OS Paenibacillus sp. FSL H8-0548.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920422 {ECO:0000313|EMBL:OMF31670.1, ECO:0000313|Proteomes:UP000187405};
RN [1] {ECO:0000313|EMBL:OMF31670.1, ECO:0000313|Proteomes:UP000187405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H8-0548 {ECO:0000313|EMBL:OMF31670.1,
RC ECO:0000313|Proteomes:UP000187405};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATPase required for the correct placement of the division
CC site. Cell division inhibitors MinC and MinD act in concert to form an
CC inhibitor capable of blocking formation of the polar Z ring septums.
CC Rapidly oscillates between the poles of the cell to destabilize FtsZ
CC filaments that have formed before they mature into polar Z rings.
CC {ECO:0000256|ARBA:ARBA00025436}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMF31670.1}.
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DR EMBL; MRTK01000021; OMF31670.1; -; Genomic_DNA.
DR RefSeq; WP_076337366.1; NZ_MRTK01000021.1.
DR AlphaFoldDB; A0A1R1D405; -.
DR STRING; 1920422.BK133_15680; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000187405; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02036; MinD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01968; minD_bact; 1.
DR PANTHER; PTHR43384:SF6; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01656; CbiA; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187405}.
FT DOMAIN 5..216
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 263 AA; 28757 MW; 8848A25556690E83 CRC64;
MGEAIVVTSG KGGVGKTTTS ANLGTALALL GKKVCMVDTD IGLRNLDVVM GLENRIIYDL
VDVAEGRCRL NQALVKDKRF DELYMLPAAQ TKDKDSVKPE QVKKMIDELK KEHDYVIIDC
PAGIEHGFRN AIAGADRAII VTTPENAAVR DADRVIGLLE QEKIPSKLII NRIRPNMMKN
GEMLDIDEIC QVLAIDLVGI VPDDEKVISA ANSGEPTVMN PTSRAAIAYR NIARRILGDM
VPLMLLDEKA GAFKRFRKFL GIG
//
